QS2_TOBAC
ID QS2_TOBAC Reviewed; 726 AA.
AC A0A1S4CB73;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Quinolinate synthase, chloroplastic {ECO:0000250|UniProtKB:Q9FGS4};
DE EC=2.5.1.72 {ECO:0000250|UniProtKB:Q9FGS4};
DE Flags: Precursor;
GN Name=QS {ECO:0000250|UniProtKB:Q9FGS4};
GN ORFNames=LOC107817199 {ECO:0000312|RefSeq:XP_016498472.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2]
RP REVIEW ON ALKALOID BIOSYNTHESIS IN NICOTIANA TABACUM.
RX PubMed=23953973; DOI=10.1016/j.phytochem.2013.06.002;
RA Dewey R.E., Xie J.;
RT "Molecular genetics of alkaloid biosynthesis in Nicotiana tabacum.";
RL Phytochemistry 94:10-27(2013).
RN [3]
RP REVIEW ON NICOTINE BIOSYNTHESIS.
RX PubMed=25582664; DOI=10.1007/s00438-015-0989-7;
RA Wang X., Bennetzen J.L.;
RT "Current status and prospects for the study of Nicotiana genomics,
RT genetics, and nicotine biosynthesis genes.";
RL Mol. Genet. Genomics 290:11-21(2015).
RN [4]
RP FUNCTION, AND PATHWAY.
RC STRAIN=cv. Burley Stella, cv. Burley TN90, cv. Virginia ITB 683, and
RC cv. Virginia K326;
RX PubMed=31276744; DOI=10.1016/j.fct.2019.110660;
RA Schorderet Weber S., Kaminski K.P., Perret J.-L., Leroy P., Mazurov A.,
RA Peitsch M.C., Ivanov N.V., Hoeng J.;
RT "Antiparasitic properties of leaf extracts derived from selected Nicotiana
RT species and Nicotiana tabacum varieties.";
RL Food Chem. Toxicol. 132:110660-110660(2019).
CC -!- FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural
CC products, leading mainly to the production of anabasine, anatabine,
CC nicotine and nornicotine, effective deterrents against herbivores with
CC antiparasitic and pesticide properties (neurotoxins); nornicotine
CC serves as the precursor in the synthesis of the carcinogen compound N'-
CC nitrosonornicotine (NNN) (PubMed:23953973, PubMed:31276744). Catalyzes
CC the condensation of iminoaspartate with dihydroxyacetone phosphate to
CC form quinolinate (By similarity). {ECO:0000250|UniProtKB:Q9FGS4,
CC ECO:0000269|PubMed:31276744, ECO:0000303|PubMed:23953973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O +
CC phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72;
CC Evidence={ECO:0000250|UniProtKB:Q9FGS4};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9FGS4};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q9FGS4};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000269|PubMed:31276744}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000250|UniProtKB:Q9FGS4}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FGS4}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q9FGS4}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 1
CC subfamily. {ECO:0000305}.
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DR RefSeq; XP_016498472.1; XM_016642986.1.
DR SMR; A0A1S4CB73; -.
DR GeneID; 107817199; -.
DR KEGG; nta:107817199; -.
DR OMA; RKTPFEP; -.
DR OrthoDB; 1016662at2759; -.
DR UniPathway; UPA00107; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008987; F:quinolinate synthetase A activity; IBA:GO_Central.
DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
DR Gene3D; 3.40.50.10800; -; 3.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
DR PANTHER; PTHR30573; PTHR30573; 1.
DR Pfam; PF02445; NadA; 1.
DR Pfam; PF02657; SufE; 1.
DR SUPFAM; SSF142754; SSF142754; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Alkaloid metabolism; Chloroplast; Iron; Iron-sulfur; Metal-binding;
KW Plastid; Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..726
FT /note="Quinolinate synthase, chloroplastic"
FT /id="PRO_0000455789"
FT ACT_SITE 133
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9FGS4"
FT BINDING 283
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 309
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 363
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 392..394
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 414
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 487
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 513..515
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 538
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 643
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
SQ SEQUENCE 726 AA; 78853 MW; DA7312AFEDEAB2EA CRC64;
MDAANLVMKS SLFSKSPCPL FSSKLIPRAP PSVFTLPSTF RPLVKCIQAS FPPNPDSKKP
SNNSTFTCSA VTSFPSQQSQ PHAPSDAKLQ LLISEFQSLV EPMDRVKRLL HYSTLLPPMD
ASFKTPENRV PGCTTQVWLN VSFDEAENRM KFLADSDSEI TKGFCACLVS LLDGATPDEV
LALKTEDLNA LNVAGLNGKG SASRANTWHN VLVSMQKRTR ALVAEREGRP RGELFPSLVI
TADGIQPQGS YAEAQARFLF PDESRVQKLA SLLKEKKIGV VAHFYMDPEV QGVLTAAQKL
WPHIHISDSL VMADKAVSMA KAGCEYISVL GVDFMSENVR AILDLAGFPE VGVYRMSDER
IGCSLADAAA SPAYLDYLKT ASTSSPSLHV VYINTSLETK AYSHELVPTI TCTSSNVVQT
ILQAFAEVPD LEVLYGPDTY MGSNIAELFT QMSTMTDEEI SAIHPLHNRI SIKSLLPRLH
YFQDGTCIVH HLFGHEVVEK INEMYGDAFL TAHFEVPGEM FSLAMEAKKR GMGVVGSTSN
ILDFIKERVE ESLNRNVDEH LQFVLGTESG MITAIVAAVG KLLGSADSSS GGAKVSVEIV
FPVSSESVTR TSTGSPLDQN KVNIIPGVAS GEGCSLHGGC ASCPYMKMNS LSSLLKVCQS
LPHGKAELSA YEAGRFSLRT PKGKQIADVG CEPVLHMRHF QATKRLPEQL INQILQPRDN
GRSSSA
